GP35 ANOAL, an abundant acidic glycoprotein of female Anopheles albimanus saliva
Salivary glands of female mosquitoes produce proteins, not completely described yet, that participate in carbohydrate and blood feeding. Here, we report an acidic glycoprotein of 35 kDa (GP35 ANOAL) secreted in the saliva of the malaria vector mosquito Anopheles albimanus. GP35 ANOAL is produced exc...
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| Veröffentlicht in: | Insect molecular biology 2007-04, Vol.16 (2), p.187-198 |
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| creator | Cázares-Raga, F.E González-Lázaro, M Montero-Solís, C González-Cerón, L Zamudio, F Martínez-Barnetche, J Torres-Monzón, J.A Ovilla-Muñoz, M Aguilar-Fuentes, J Rodríguez, M.H de la Cruz Hernández-Hernández, F |
| description | Salivary glands of female mosquitoes produce proteins, not completely described yet, that participate in carbohydrate and blood feeding. Here, we report an acidic glycoprotein of 35 kDa (GP35 ANOAL) secreted in the saliva of the malaria vector mosquito Anopheles albimanus. GP35 ANOAL is produced exclusively in the distal lateral lobes of adult female salivary glands, it has a pI of 4.45 and is negatively stained by regular silver stain. An 888 bp cDNA clone encoding a predicted product of 240 amino acids has a signal peptide, potential post-translational modification sites, and a disintegrin signature RGD. The GP35 ANOAL sequence depicts high similarities with the 30 kDa saliva allergen of Aedes aegypti, 30 kDa allergen-like hypothetical proteins, and GE-rich proteins present in several Anopheles species, as well as in Ae. albopictus and Culex pipiens quinquefasciatus. The function of this protein family is still unknown. |
| doi_str_mv | 10.1111/j.1365-2583.2006.00712.x |
| format | Article |
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Here, we report an acidic glycoprotein of 35 kDa (GP35 ANOAL) secreted in the saliva of the malaria vector mosquito Anopheles albimanus. GP35 ANOAL is produced exclusively in the distal lateral lobes of adult female salivary glands, it has a pI of 4.45 and is negatively stained by regular silver stain. An 888 bp cDNA clone encoding a predicted product of 240 amino acids has a signal peptide, potential post-translational modification sites, and a disintegrin signature RGD. The GP35 ANOAL sequence depicts high similarities with the 30 kDa saliva allergen of Aedes aegypti, 30 kDa allergen-like hypothetical proteins, and GE-rich proteins present in several Anopheles species, as well as in Ae. albopictus and Culex pipiens quinquefasciatus. 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Here, we report an acidic glycoprotein of 35 kDa (GP35 ANOAL) secreted in the saliva of the malaria vector mosquito Anopheles albimanus. GP35 ANOAL is produced exclusively in the distal lateral lobes of adult female salivary glands, it has a pI of 4.45 and is negatively stained by regular silver stain. An 888 bp cDNA clone encoding a predicted product of 240 amino acids has a signal peptide, potential post-translational modification sites, and a disintegrin signature RGD. The GP35 ANOAL sequence depicts high similarities with the 30 kDa saliva allergen of Aedes aegypti, 30 kDa allergen-like hypothetical proteins, and GE-rich proteins present in several Anopheles species, as well as in Ae. albopictus and Culex pipiens quinquefasciatus. The function of this protein family is still unknown.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anopheles - genetics</subject><subject>Anopheles - growth & development</subject><subject>Anopheles - metabolism</subject><subject>Anopheles albimanus</subject><subject>Base Sequence</subject><subject>Culicidae</subject><subject>Female</subject><subject>glycoprotein</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>GP35</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>mosquito</subject><subject>RNA, Messenger - metabolism</subject><subject>salivary glands</subject><subject>Salivary Glands - metabolism</subject><subject>sex-specific</subject><issn>0962-1075</issn><issn>1365-2583</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkF1v0zAUhi0EYt3gL4DFBVdL8Ef8JXFTBpRJ7TYxJi6PnNgeKWlS4gbaf49DqiFxhW9syc_76pwHIUxJTtN5s84plyJjQvOcESJzQhRl-f4Rmj18PEYzYiTLKFHiBJ3GuCaEaCPNU3RCFTNaCD1DN4sbLvD86nq-PMe2xbYcWmfbHbZV7eoK3zeHqtv23c7XLe4CDn5jG4_nbbf95hsfsW3KemPbIeJom_qnfYaeBNtE__x4n6G7jx--XHzKlteLy4v5MqsKIVjGPE3TOFbxwntBJXPMBVd4FwQriWWVC0FJwXhhOC2p0qSsgjDSKi29NIafoddTbxrux-DjDjZ1rHzT2NZ3QwRFmDCGyAS--gdcd0PfptmAkUIxbtQI6Qmq-i7G3gfY9mmt_gCUwKgc1jCahdEsjMrhj3LYp-iLY_9Qbrz7Gzw6TsDbCfhVN_7w38VwuXqXHimeTfE67vz-IW777yAVVwK-Xi1Ar8j7z8tbCavEv5z4YDuw930d4e6WEcpTryg04_w3OaylOA</recordid><startdate>200704</startdate><enddate>200704</enddate><creator>Cázares-Raga, F.E</creator><creator>González-Lázaro, M</creator><creator>Montero-Solís, C</creator><creator>González-Cerón, L</creator><creator>Zamudio, F</creator><creator>Martínez-Barnetche, J</creator><creator>Torres-Monzón, J.A</creator><creator>Ovilla-Muñoz, M</creator><creator>Aguilar-Fuentes, J</creator><creator>Rodríguez, M.H</creator><creator>de la Cruz Hernández-Hernández, F</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200704</creationdate><title>GP35 ANOAL, an abundant acidic glycoprotein of female Anopheles albimanus saliva</title><author>Cázares-Raga, F.E ; González-Lázaro, M ; Montero-Solís, C ; González-Cerón, L ; Zamudio, F ; Martínez-Barnetche, J ; Torres-Monzón, J.A ; Ovilla-Muñoz, M ; Aguilar-Fuentes, J ; Rodríguez, M.H ; de la Cruz Hernández-Hernández, F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4552-2e1008d2c34ee5162d2dfd4edf52b0a2cdff765234931b1780bcf596a786e6993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anopheles - genetics</topic><topic>Anopheles - growth & development</topic><topic>Anopheles - metabolism</topic><topic>Anopheles albimanus</topic><topic>Base Sequence</topic><topic>Culicidae</topic><topic>Female</topic><topic>glycoprotein</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - metabolism</topic><topic>GP35</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>mosquito</topic><topic>RNA, Messenger - metabolism</topic><topic>salivary glands</topic><topic>Salivary Glands - metabolism</topic><topic>sex-specific</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cázares-Raga, F.E</creatorcontrib><creatorcontrib>González-Lázaro, M</creatorcontrib><creatorcontrib>Montero-Solís, C</creatorcontrib><creatorcontrib>González-Cerón, L</creatorcontrib><creatorcontrib>Zamudio, F</creatorcontrib><creatorcontrib>Martínez-Barnetche, J</creatorcontrib><creatorcontrib>Torres-Monzón, J.A</creatorcontrib><creatorcontrib>Ovilla-Muñoz, M</creatorcontrib><creatorcontrib>Aguilar-Fuentes, J</creatorcontrib><creatorcontrib>Rodríguez, M.H</creatorcontrib><creatorcontrib>de la Cruz Hernández-Hernández, F</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Insect molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cázares-Raga, F.E</au><au>González-Lázaro, M</au><au>Montero-Solís, C</au><au>González-Cerón, L</au><au>Zamudio, F</au><au>Martínez-Barnetche, J</au><au>Torres-Monzón, J.A</au><au>Ovilla-Muñoz, M</au><au>Aguilar-Fuentes, J</au><au>Rodríguez, M.H</au><au>de la Cruz Hernández-Hernández, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>GP35 ANOAL, an abundant acidic glycoprotein of female Anopheles albimanus saliva</atitle><jtitle>Insect molecular biology</jtitle><addtitle>Insect Mol Biol</addtitle><date>2007-04</date><risdate>2007</risdate><volume>16</volume><issue>2</issue><spage>187</spage><epage>198</epage><pages>187-198</pages><issn>0962-1075</issn><eissn>1365-2583</eissn><abstract>Salivary glands of female mosquitoes produce proteins, not completely described yet, that participate in carbohydrate and blood feeding. Here, we report an acidic glycoprotein of 35 kDa (GP35 ANOAL) secreted in the saliva of the malaria vector mosquito Anopheles albimanus. GP35 ANOAL is produced exclusively in the distal lateral lobes of adult female salivary glands, it has a pI of 4.45 and is negatively stained by regular silver stain. An 888 bp cDNA clone encoding a predicted product of 240 amino acids has a signal peptide, potential post-translational modification sites, and a disintegrin signature RGD. The GP35 ANOAL sequence depicts high similarities with the 30 kDa saliva allergen of Aedes aegypti, 30 kDa allergen-like hypothetical proteins, and GE-rich proteins present in several Anopheles species, as well as in Ae. albopictus and Culex pipiens quinquefasciatus. The function of this protein family is still unknown.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>17298558</pmid><doi>10.1111/j.1365-2583.2006.00712.x</doi><tpages>12</tpages></addata></record> |
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| identifier | ISSN: 0962-1075 |
| ispartof | Insect molecular biology, 2007-04, Vol.16 (2), p.187-198 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amino Acid Sequence Animals Anopheles - genetics Anopheles - growth & development Anopheles - metabolism Anopheles albimanus Base Sequence Culicidae Female glycoprotein Glycoproteins - genetics Glycoproteins - metabolism GP35 Insect Proteins - genetics Insect Proteins - metabolism Molecular Sequence Data mosquito RNA, Messenger - metabolism salivary glands Salivary Glands - metabolism sex-specific |
| title | GP35 ANOAL, an abundant acidic glycoprotein of female Anopheles albimanus saliva |
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